Primary amine oxidase precursor - Lens culinaris (Lentil)

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Reviewed, UniProtKB/Swiss-Prot P49252 (AMO_LENCU)

Last modified September 22, 2009. Version 63. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names	Recommended name: Primary amine oxidase EC=1.4.3.21 Alternative name(s): Amine oxidase [copper-containing]
Organism	Lens culinaris (Lentil) (Cicer lens)
Taxonomic identifier	3864 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Lens

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Protein attributes

Sequence length	667 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	RCH₂NH₂ + H₂O + O₂ = RCHO + NH₃ + H₂O₂.
Cofactor	Binds 1 copper ion per subunit. Contains 1 topaquinone per subunit By similarity.
Subunit structure	Homodimer.
Post-translational modification	Glycosylated; contains two carbohydrate chains per monomer. Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue By similarity.
Sequence similarities	Belongs to the copper/topaquinone oxidase family.
Sequence caution	The sequence CAA45526.1 differs from that shown. Reason: Frameshift at several positions.

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Ontologies

Keywords
Domain	Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein TPQ
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	amine metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	amine oxidase activity Inferred from electronic annotation. Source: EC copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

‹1 – 18

›18

Ref.1

Chain

19 – 667

649

Primary amine oxidase

PRO_0000035679

Sites

Active site

318

Proton acceptor By similarity

Active site

405

Schiff-base intermediate with substrate; via topaquinone By similarity

Metal binding

460

Copper By similarity

Metal binding

462

Copper By similarity

Metal binding

469

Manganese By similarity

Metal binding

470

Manganese; via carbonyl oxygen By similarity

Metal binding

471

Manganese By similarity

Metal binding

610

Manganese By similarity

Metal binding

611

Manganese; via carbonyl oxygen By similarity

Metal binding

621

Copper By similarity

Amino acid modifications

Modified residue

405

2',4',5'-topaquinone By similarity

Glycosylation

149

N-linked (GlcNAc...) Potential

Glycosylation

252

N-linked (GlcNAc...) Potential

Glycosylation

382

N-linked (GlcNAc...) Potential

Glycosylation

576

N-linked (GlcNAc...) Potential

Disulfide bond

155 ↔ 176

By similarity

Disulfide bond

337 ↔ 363

By similarity

Experimental info

Sequence conflict

492 – 496

GGSKR → EVQE in CAA45526. Ref.1

Sequence conflict

575

Y → N AA sequence Ref.1

Sequence conflict

651

V → A AA sequence Ref.1

Sequence conflict

658

R → I AA sequence Ref.1

Non-terminal residue

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Sequences

Sequence

Length

Mass (Da)

Tools

P49252-1 [UniParc].

Last modified November 23, 2004. Version 3.
Checksum: ED9A415C7E4F7AEC
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FASTA

667

75,558

        10         20         30         40         50         60 
KFALFSVLTL LSFHAVFSFT PLHTQHPLDP ITKEEFLAVQ TIVQNKYPIS NNKLAFHYIG 

        70         80         90        100        110        120 
VDDPEKDLVL KYETSPTLIS IPRKIFVVAI INSQTHEILI DLTIKSIVSD NIHNGYGFPV 

       130        140        150        160        170        180 
LSAAEQFLAI DLPLKYPPFI ASVNKRGLNI SEIVCSSFTM GWFGEEKNSR TVRVDCFMKE 

       190        200        210        220        230        240 
STVNIYVRPI TGITIVADLD LMKIVEYHDR DTEAVPTAEN TEYQVSKQSP PFGPKQHSLT 

       250        260        270        280        290        300 
SHQPQGPGFQ INGTSVSWAN WKFHIGFDVR AGIVISLASI YDLEKHKSRR VLYKGYISEL 

       310        320        330        340        350        360 
FVPYQDPTEE FYFKTFFDSG EFGFGLSTVS LIPNRDCPPH AQFIDTYIHS ADGTPIFLEN 

       370        380        390        400        410        420 
AICVFEQYGN IMWRHTETGI PNESIEESRT EVDLAIRTVV TVGNYDNVLD WEFKTSGWMK 

       430        440        450        460        470        480 
PSIALSGILE IKGTNIKHKD EIKEEIHGKL VSANSIGIYH DHFYIYYLDF DIDGTQNSFE 

       490        500        510        520        530        540 
KTSLKTVRIV DGGSKRKSYW TTETQTAKTE SDAKITIGLA PAELVVVNPN IKTAVGNEVG 

       550        560        570        580        590        600 
YRLIPAIPAH PLLTEDDYPQ IRGAFTNYNV WVTPYNRTEK WAGGLYVDHS RGDDTLAVWT 

       610        620        630        640        650        660 
KKNREIVNKD IVMWHVVGIH HVPAQEDFPI MPLLSTSFEL RPTNFFERNP VLKTLPPRDF 


TWPGCSN

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References

[1]	"cDNA-derived amino-acid sequence of lentil seedlings' amine oxidase." Rossi A., Petruzzelli R., Finazzi Agro A. FEBS Lett. 301:253-257(1992) [PubMed: 1577161] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-66 AND 543-562. Tissue: Seedling.
[2]	"Cloning and molecular analysis of the pea seedling copper amine oxidase." Tipping A.J., McPherson M.J. J. Biol. Chem. 270:16939-16946(1995) [PubMed: 7622512] [Abstract] Cited for: SEQUENCE REVISION TO 444-667.
[3]	McPherson M.J. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Copper-containing plant oxidases." Agro A.F., Rossi A. Biochem. Soc. Trans. 20:369-373(1992) [PubMed: 1397633] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-35; 258-276 AND 360-377.

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Cross-references

Sequence databases
	X64201 mRNA. Translation: CAA45526.1. Frameshift. S78994 mRNA. Translation: AAB34918.3.
PIR	S21139.
3D structure databases
HSSP	HSSP built from PDB template 1KSI based on UniProtKB Q43077.
SMR	P49252. Positions 25-665.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.4.3.6. 1096.
Family and domain databases
InterPro	IPR000269. Cu_amine_oxidase. IPR015798. Cu_amine_oxidase_C. IPR015800. Cu_amine_oxidase_N2. IPR015801. Cu_amine_oxidase_N2/3. IPR015802. Cu_amine_oxidase_N3. [Graphical view]
Gene3D	G3DSA:3.10.450.40. CuNH_oxidase. 2 hits. G3DSA:2.70.98.20. Lyase_8_central. 1 hit.
PANTHER	PTHR10638. CuNH_oxidase. 1 hit.
Pfam	PF01179. Cu_amine_oxid. 1 hit. PF02727. Cu_amine_oxidN2. 1 hit. PF02728. Cu_amine_oxidN3. 1 hit. [Graphical view]
PROSITE	PS01164. COPPER_AMINE_OXID_1. 1 hit. PS01165. COPPER_AMINE_OXID_2. False negative. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

AMO_LENCU

Accession

Primary (citable) accession number: P49252
Secondary accession number(s): Q9LD03

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	November 23, 2004
Last modified:	September 22, 2009
This is version 63 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents